MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily

  title={MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily},
  author={Yue Guan and Raymond C. Manuel and Andrew S. Arvai and Sudip S. Parikh and Clifford D. Mol and Jeffrey H. Miller and R. Stephen Lloyd and John A. Tainer},
  journal={Nature Structural Biology},
The DNA glycosylase MutY, which is a member of the Helix-hairpin-Helix (HhH) DNA glycosylase superfamily, excises adenine from mispairs with 8-oxoguanine and guanine. High-resolution crystal structures of the MutY catalytic core (cMutY), the complex with bound adenine, and designed mutants reveal the basis for adenine specificity and glycosyl bond cleavage chemistry. The two cMutY helical domains form a positively-charged groove with the adenine-specific pocket at their interface. The Watson… 

Reaction Intermediates in the Catalytic Mechanism of Escherichia coli MutY DNA Glycosylase*

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3-methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member

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Atomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylase

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Crystallizing thoughts about DNA base excision repair.

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The crystal structure of an NAD+‐dependent DNA ligase from Thermus filiformis, a 667 residue multidomain protein, has been determined by the multiwavelength anomalous diffraction (MAD) method and reveals highly modular architecture and a unique circular arrangement of its four distinct domains.

Flipping Duplex DNA Inside Out

Enhanced cross-linking was observed in the single strand experiments, suggesting that neither the duplex context nor the mismatch with adenine is required for recognition of the 8-oxoguanine moiety.



MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III

The mutY gene of Escherichia coli, which codes for an adenine glycosylase that excises the adenine of a G-A mispair, has been cloned and sequenced. The mutY gene codes for a protein of 350 amino

Crystal structure of a DNA duplex containing 8-hydroxydeoxyguanine-adenine base pairs.

The crystal structure of the oligonucleotide d(CGCAAATTO8GGCG), containing the chemically modified base 8-hydroxydeoxyguanine (O8G), has been determined at 2.5-A resolution and refined to a

Identification of the Structural and Functional Domains of MutY, an Escherichia coli DNA Mismatch Repair Enzyme*

The structure predicted by molecular modeling indicates that the region of MutY (Met1-Trp216), which is homologous to endonuclease III exhibits a two domain structure, even though this portion is resistant to proteolysis by trypsin.

Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity, and fidelity.

Crystal structures of human pol beta complexed with blunt-ended segments of DNA show that, although the crystals belong to a different space group, the DNA is nevertheless bound in the pol beta binding channel in the same way as the DNA in previously reported structures of rat pol beta complexes with a template-primer and ddCTP.

Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III.

The crystal structure of the DNA repair enzyme endonuclease III reveals an unusual fold and a new biological function for [4Fe-4S] clusters and provides a structural basis for studying recognition of damaged DNA and the N-glycosylase and apurinic/apyrimidinic-lyase mechanisms.

Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil‐DNA glycosylase with DNA

UDG binds to AP sites more tightly and more rapidly than to uracil‐containing DNA, and thus may protect cells sterically from AP site toxicity, and AP site binding may couple damage‐specific and damage‐general steps of BER without requiring direct protein–protein interactions.

Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY

It is shown for the first time that deletion of 125 amino acids at the C-terminus of MutY generates a stable catalytic domain which retains the functional identity of the intact protein.